DSE

The protein encoded by this gene is a tumor-rejection antigen. It is localized to the endoplasmic reticulum and functions to convert D-glucuronic acid to L-iduronic acid during the biosynthesis of dermatan sulfate. This antigen possesses tumor epitopes capable of inducing HLA-A24-restricted and tumor-specific cytotoxic T lymphocytes in cancer patients and may be useful for specific immunotherapy. Mutations in this gene cause inmusculocontractural Ehlers-Danlos syndrome. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 9, and a paralogous gene exists on chromosome 18. [provided by RefSeq, Apr 2016]

Full Name

Dermatan Sulfate Epimerase

Research Area

Converts D-glucuronic acid to L-iduronic acid (IdoUA) residues. Plays an important role in the biosynthesis of the glycosaminoglycan/mucopolysaccharide dermatan sulfate.

Biological Process

Chondroitin sulfate biosynthetic process Source: UniProtKB-UniPathway
Chondroitin sulfate metabolic process Source: GO_Central
Dermatan sulfate biosynthetic process Source: UniProtKB
Dermatan sulfate metabolic process Source: GO_Central
Heparan sulfate proteoglycan biosynthetic process Source: UniProtKB-UniPathway

Cellular Location

Golgi apparatus membrane; Endoplasmic reticulum membrane; Microsome membrane; Cytoplasmic vesicle membrane

Involvement in disease

Ehlers-Danlos syndrome, musculocontractural type 2 (EDSMC2):
A form of Ehlers-Danlos syndrome characterized by progressive multisystem manifestations, including joint dislocations and deformities, skin hyperextensibility, skin bruisability and fragility with recurrent large subcutaneous hematomas, cardiac valvular, respiratory, gastrointestinal, and ophthalmologic complications. Motor developmental delay is associated with muscle hypoplasia, muscle weakness, and an abnormal muscle fiber pattern in histology in adulthood.

Topology

Lumenal: 23-902
Helical: 903-923
Cytoplasmic: 924-933
Helical: 934-954
Lumenal: 955-958

PTM

N-glycosylated (PubMed:19004833, Ref. 7). Glycosylation is important for enzymatic activity (PubMed:19004833).